PDBsum entry 2x98

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
430 a.a. *
PO4 ×2
_CL ×13
_ZN ×4
_MG ×11
_NA ×2
Waters ×943
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: H.Salinarum alkaline phosphatase
Structure: Alkaline phosphatase. Chain: a, b. Fragment: residues 44-474. Ec:
Source: Halobacterium salinarum. Organism_taxid: 478009. Strain: r1. Expressed in: halobacterium salinarum. Expression_system_taxid: 478009.
1.70Å     R-factor:   0.163     R-free:   0.197
Authors: A.Wende,P.Johansson,M.Grininger,D.Oesterhelt
Key ref: A.Wende et al. (2010). Structural and biochemical characterization of a halophilic archaeal alkaline phosphatase. J Mol Biol, 400, 52-62. PubMed id: 20438737
14-Mar-10     Release date:   19-May-10    
Supersedes: 2w0y
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
B0R9W3  (B0R9W3_HALS3) -  Alkaline phosphatase
473 a.a.
430 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Alkaline phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A phosphate monoester + H2O = an alcohol + phosphate
phosphate monoester
+ H(2)O
= alcohol
Bound ligand (Het Group name = PO4)
corresponds exactly
      Cofactor: Magnesium; Zinc
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   2 terms 
  Biochemical function     catalytic activity     5 terms  


J Mol Biol 400:52-62 (2010)
PubMed id: 20438737  
Structural and biochemical characterization of a halophilic archaeal alkaline phosphatase.
A.Wende, P.Johansson, R.Vollrath, M.Dyall-Smith, D.Oesterhelt, M.Grininger.
Phosphate is an essential component of all cells that must be taken up from the environment. Prokaryotes commonly secrete alkaline phosphatases (APs) to recruit phosphate from organic compounds by hydrolysis. In this study, the AP from Halobacterium salinarum, an archaeon that lives in a saturated salt environment, has been functionally and structurally characterized. The core fold and the active-site architecture of the H. salinarum enzyme are similar to other AP structures. These generally form dimers composed of dominant beta-sheet structures sandwiched by alpha-helices and have well-accessible active sites. The surface of the enzyme is predicted to be highly negatively charged, like other proteins of extreme halophiles. In addition to the conserved core, most APs contain a crown domain that strongly varies within species. In the H. salinarum AP, the crown domain is made of an acyl-carrier-protein-like fold. Different from other APs, it is not involved in dimer formation. We compare the archaeal AP with its bacterial and eukaryotic counterparts, and we focus on the role of crown domains in enhancing protein stability, regulating enzyme function, and guiding phosphoesters into the active-site funnel.